Genetic analysis, structural modeling, and direct coupling analysis suggest a mechanism for phosphate signaling in Escherichia coli

11 1 0
Genetic analysis, structural modeling, and direct coupling analysis suggest a mechanism for phosphate signaling in Escherichia coli

Đang tải... (xem toàn văn)

Tài liệu hạn chế xem trước, để xem đầy đủ mời bạn chọn Tải xuống

Thông tin tài liệu

Proper phosphate signaling is essential for robust growth of Escherichia coli and many other bacteria. The phosphate signal is mediated by a classic two component signal system composed of PhoR and PhoB.

ibutions SGG planned, performed experiments, prepared, and edited the manuscript JM performed DCA, helped with analysis of data, and aided in preparing the manuscript TD, TR, and ME helped in the scanning mutagenesis PR helped with bioinformatic experimental planning and analysis WRM designed experiments, conducted experiments, aided in data analysis, and aided in preparing and editing the manuscript Acknowledgements We thank Kathryn Hanks, Alex Cummock, Evan Christensen, Bethany Evans, Gregory Bowden, and Michael Barrus for help with sequence collection and mutant characterization This work was supported by Public Health Service grant R15GM96222 from the National Institute of General Medical Sciences Declarations The publication costs for this article were funded by the Department of Microbiology and Molecular Biology at Brigham Young University, the College of Life Sciences at Brigham Young University, and the Public Health Service grant R15GM96222 from the National Institute of General Medical Sciences Gardner et al BMC Genetics 2015, 16(Suppl 2):S2 http://www.biomedcentral.com/1471-2156/16/S2/S2 Page 11 of 11 This article has been published as part of BMC Genetics Volume 16 Supplement 2, 2015: Selected articles from The 11th Annual Biotechnology and Bioinformatics Symposium (BIOT-2014): Genetics The full contents of the supplement are available online at http://www.biomedcentral.com/ bmcgenet/supplements/16/S2 19 Authors’ details Microbiology and Molecular Biology Department, Brigham Young University, Provo, UT, USA 2Department of Biology, Brigham Young University, Provo, UT, USA 20 Published: 23 April 2015 21 References Wanner BL: Phosphorus assimilation and control of the phosphate regulon In Escherichia coli and Salmonella: cellular and molecular biology Washington D C.: American Society for Microbiology;Neidhardt FC, III RC, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE 1996:1357-1381 Chekabab SM, Harel J, Dozois CM: Interplay between genetic regulation of phosphate homeostasis and bacterial virulence Virulence 2014, 5(5) Lamarche MG, Wanner BL, Crepin S, Harel J: The phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesis FEMS Microbiol Rev 2008, 32(3):461-473 Taylor BL, Zhulin IB: PAS domains: internal sensors of oxygen, redox potential, and light Microbiology and molecular biology reviews : MMBR 1999, 63(2):479-506 Steed PM, Wanner BL: Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon J Bacteriol 1993, 175(21):6797-6809 Haldimann A, Daniels LL, Wanner BL: Use of new methods for construction of tightly regulated arabinose and rhamnose promoter fusions in studies of the Escherichia coli phosphate regulon J Bacteriol 1998, 180(5):1277-1286 Rice CD, Pollard JE, Lewis ZT, McCleary WR: Employment of a promoterswapping technique shows that PhoU modulates the activity of the PstSCAB2 ABC transporter in Escherichia coli Appl Environ Microbiol 2009, 75(3):573-582 Gardner SG, Johns KD, Tanner R, McCleary WR: The PhoU protein from Escherichia coli interacts with PhoR, PstB, and metals to form a phosphate-signaling complex at the membrane J Bacteriol 2014, 196(9):1741-1752 Buron-Barral MC, Gosink KK, Parkinson JS: Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer J Bacteriol 2006, 188(10):3477-3486 10 Studdert CA, Parkinson JS: Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies Proceedings of the National Academy of Sciences of the United States of America 2005, 102(43):15623-15628 11 Datsenko KA, Wanner BL: One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products Proc Natl Acad Sci USA 2000, 97:6640-6645 12 Kozakov D, Brenke R, Comeau SR, Vajda S: PIPER: an FFT-based protein docking program with pairwise potentials Proteins 2006, 65(2):392-406 13 Comeau SR, Gatchell DW, Vajda S, Camacho CJ: ClusPro: an automated docking and discrimination method for the prediction of protein complexes Bioinformatics 2004, 20(1):45-50 14 Comeau SR, Gatchell DW, Vajda S, Camacho CJ: ClusPro: a fully automated algorithm for protein-protein docking Nucleic acids research 2004, 32(Web Server):W96-99 15 Kozakov D, Beglov D, Bohnuud T, Mottarella S, Xia B, Hall DR, Vajda S: How good is automated protein docking? Proteins: Structure, Function, and Bioinformatics 2013, 81(12):2159-2166 16 Wang C, Sang J, Wang J, Su M, Downey JS, Wu Q, Wang S, Cai Y, Xu X, Wu J, et al: Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains PLoS biology 2013, 11(2):e1001493 17 Madej T, Addess KJ, Fong JH, Geer LY, Geer RC, Lanczycki CJ, Liu C, Lu S, Marchler-Bauer A, Panchenko AR, et al: MMDB: 3D structures and 22 18 23 24 25 26 27 28 29 30 31 32 33 34 35 macromolecular interactions Nucleic acids research 2012, 40(Database): D461-464 Kelley LA, Sternberg MJ: Protein structure prediction on the Web: a case study using the Phyre server Nature protocols 2009, 4(3):363-371 Morcos F, Pagnani A, Lunt B, Bertolino A, Marks DS, Sander C, Zecchina R, Onuchic JN, Hwa T, Weigt M: Direct-coupling analysis of residue coevolution captures native contacts across many protein families Proceedings of the National Academy of Sciences of the United States of America 2011, 108(49):E1293-1301 Torriani A, Rothman F: Mutants of Escherichia coli constitutive for alkaline phosphatase J Bacteriol 1961, 81:835-836 Garen A, Otsuji N: Isolation of a Protein Specified by a Regulator Gene J Mol Biol 1964, 8:841-852 Zuckier G, Torriani A: Genetic and physiological tests of three phosphatespecific transport mutants of Escherichia coli J Bacteriol 1981, 145(3):1249-1256 Amemura M, Shinagawa H, Makino K, Otsuji N, Nakata A: Cloning of and complementation tests with alkaline phosphatase regulatory genes (phoS and phoT) of Escherichia coli J Bacteriol 1982, 152(2):692-701 Muda M, Rao NN, Torriani A: Role of PhoU in phosphate transport and alkaline phosphatase regulation J Bacteriol 1992, 174(24):8057-8064 Dwyer RS, Ricci DP, Colwell LJ, Silhavy TJ, Wingreen NS: Predicting functionally informative mutations in Escherichia coli BamA using evolutionary covariance analysis Genetics 2013, 195(2):443-455 Liu Y, Eyal E, Bahar I: Analysis of correlated mutations in HIV-1 protease using spectral clustering Bioinformatics 2008, 24(10):1243-1250 Liu Y, Bahar I: Sequence evolution correlates with structural dynamics Mol Biol Evol 2012, 29(9):2253-2263 Clark GW, Ackerman SH, Tillier ER, Gatti DL: Multidimensional mutual information methods for the analysis of covariation in multiple sequence alignments BMC bioinformatics 2014, 15:157 Simonetti FL, Teppa E, Chernomoretz A, Nielsen M, Marino Buslje C: MISTIC: Mutual information server to infer coevolution Nucleic acids research 2013, 41(Web Server):W8-14 Mahony S, Auron PE, Benos PV: Inferring protein-DNA dependencies using motif alignments and mutual information Bioinformatics 2007, 23(13):i297-304 Weil P, Hoffgaard F, Hamacher K: Estimating sufficient statistics in coevolutionary analysis by mutual information Computational biology and chemistry 2009, 33(6):440-444 Zhang S, McDonald PW, Thompson TA, Dennis AF, Akopov A, Kirkness EF, Patton JT, McDonald SM: Analysis of human rotaviruses from a single location over an 18-year time span suggests that protein coadaption influences gene constellations Journal of virology 2014, 88(17):9842-9863 Dago AE, Schug A, Procaccini A, Hoch JA, Weigt M, Szurmant H: Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis Proceedings of the National Academy of Sciences of the United States of America 2012, 109(26): E1733-1742 Albanesi D, Martin M, Trajtenberg F, Mansilla MC, Haouz A, Alzari PM, de Mendoza D, Buschiazzo A: Structural plasticity and catalysis regulation of a thermosensor histidine kinase Proceedings of the National Academy of Sciences of the United States of America 2009, 106(38):16185-16190 Carmany DO, McCleary WR: Genetic and biochemical studies of phosphate activity of PhoR J Bacteriol 2003, 185:1112-1115 doi:10.1186/1471-2156-16-S2-S2 Cite this article as: Gardner et al.: Genetic analysis, structural modeling, and direct coupling analysis suggest a mechanism for phosphate signaling in Escherichia coli BMC Genetics 2015 16(Suppl 2):S2 ... Silhavy TJ, Wingreen NS: Predicting functionally informative mutations in Escherichia coli BamA using evolutionary covariance analysis Genetics 2013, 195(2):443-455 Liu Y, Eyal E, Bahar I: Analysis. .. Bacteriol 2003, 185:1112-1115 doi:10.1186/1471-2156-16-S2-S2 Cite this article as: Gardner et al.: Genetic analysis, structural modeling, and direct coupling analysis suggest a mechanism for phosphate. .. transport mutants of Escherichia coli J Bacteriol 1981, 145(3):1249-1256 Amemura M, Shinagawa H, Makino K, Otsuji N, Nakata A: Cloning of and complementation tests with alkaline phosphatase regulatory

Ngày đăng: 27/03/2023, 04:15

Mục lục

  • Abstract

    • Background

    • Results

    • Conclusions

    • Background

    • Methods

      • Strains, plasmids, and reconstructing of signaling system

      • Growth of PhoU A147E mutant

      • Alkaline phosphatase assays

      • BACTH and β-galactosidase assays for scanning mutagenesis

      • Protein structure modeling and protein docking modeling

      • Direct coupling analysis

      • Results and discussion

      • Conclusions

      • Competing interests

      • Authors’ contributions

      • Acknowledgements

      • Declarations

      • Authors’ details

      • References

Tài liệu cùng người dùng

Tài liệu liên quan